http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
열전소자의 냉온기능을 이용한 제어패널용 제습기 설계 및 구현
장재철(Jae Chul Jang) 산업기술교육훈련학회 2015 산업기술연구논문지 (JITR) Vol.20 No.4
This paper, is to prevent failure due to moisture in the industrial control panels. Dehumidifier is operate when measuring the internal temperature of the panel, temperature is higher(during operation) thermal module cooling(cooling dehumidification) to dehumidify and low(shutdown) a thermoelectric module heat(dehumidifying heat) to remove moisture. Dehumidifier is implemented using thermoelectric module to controller a proportional of the temperature and humidity. Inside sensor is measuring temperature and humidity in order to protect the PCB circuit. Thermoelectric module according to the model size and the property is also a very important design element to the heat sink structure to maintain a proper heat resistance and vary according to the type of Module. By implementing the dehumidifier for control panel functions of the thermoelectric elements using a cold was confirmed that no noise, vibration-free, can be an effective dehumidifier by a low energy consumption of the local space.
질산화 작용이 있는 Aeromonas hydrophila의 동정 및 특성
엄미나,장재철,유영희,지의상 한국식품영양학회 2000 韓國食品營養學會誌 Vol.13 No.6
폐수처리 중 생물학적 처리에 활용할 수 있는 질소분해 능력을 가진 미생물을 분리하여 동정하고자 경기도내 하천 6지점에서 채취한 시료로부터 50개 균주를 선별하였다. 형태학적, 생화학적 및 배양학적 실험결과 Bergey's mannual of systematic bacteriology의 색인을 통하여 Aeromonas hydrophila로 동정하였다. Aeromonas hydrophila(AH-1). (AH-3), (AH-4), (AH-6) 균이 질산화 능력이 우수하였다. 4개 균주 모두 amoxillin, ampicillin, cephalothin과 ticarcillin에 내성을 나타내었다. 본 실험에서 분리한 .Aeromonas hydrophila의 질산화의 최적조건은 균 농도 1.0×l0exp(6) cells/ml, 배양온도 37℃로 나타났다. For the purpose of the isolation of microorganisms which have the capability of nitrification, we isolated the microorganisms in 6 samples collected from the stream of Kyonggi area. 60 strains were isolated. The selected strain were identified as a Aeromonas hydrophila based on the data obtained from the morphological, biochemical and cultural characteristics defined experiments. Among them Aeromonas hydrophila (AH-1), (AH-3), (AH-4), (AH-6) showed the highest nitrification capability. All isolates were resistant to amoxillin, ampicillin, cephalothin and ticarcillin. Optimum culture conditions of isolates were 37℃ and 1×10exp(8) cells/ml for 4 hours in the nitrate medium.
金鏞揮,張在哲,吳錫興 전북대학교 농업과학기술연구소 1984 農大論文集 Vol.15 No.-
Polyphenol oxidase in japanese apricot (Prunur mume Sies. er Zucc) was isolated, purified and its some properties were studied. The enzyme was purified through ammonium sulfate precipitation and DEAE-cellulose column chromatography. The activity of the purified enzyme was 1,285.10 units/mg protein and final purification and yield were 42.10 fold and 15.10%, respectively. The polyphenol oxidase activity decreased sharply during the first three days at 30℃, then decreased slowly as the storage was prolonged. At 4℃, the activity appeared to be relatively stable over 3-day period before the activity began to decline slowly. The optimum pH and temperature were 6.5 and 30℃, respectively. The enzyme was almost stable within the pH range 3.5-5.5 and under the temperature of 35℃ for 15 min., but unstable over the temperature of 40℃. ; losing about 93% of the activity at 60℃ for 15 min. The substrate specificity of the japanese apricot polyphenol oxidase showed high affinity toward o-diphenolic compounds, especially catechol, although it showed affinity toward trihydroxyphenolic compounds, but inactive toward m-diphenol, p-diphenol and monophenols. The enzyme Km value was 9.09mM with catechol as substrate. Inhibitor studies indicated that sodium diethyldithiocarbamate and L-ascorbic acid were most potent. Cu++, Mg++, Ca++ and Fe++ activated slightly the enzyme activity but Zn++, Hg++ inhibited, at 1mM concentration. Cu++ activated the enzyme action at 0.1mM, 1mM, 2mM but inhibited 5mM, 10mM and had no influence at below 0.01mM. The spectrum for catechol showed a sharp peak maximizing at 275 nm. The absorption spectrum of the purifled enzyme showed a typical maximum of 280 nm. The absorption spectrum for the product of the reaction between catechol and japanese apricot polyphenol oxidase was investigated. The absorption maximum occurred at 420 nm.